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Volumn 32, Issue 2, 2003, Pages 205-211

NADH oxidase from Lactobacillus brevis: A new catalyst for the regeneration of NAD

Author keywords

Lactobacillus; NADH oxidase; Oxidative resolution of racemates; Primary structure; Regeneration of NAD

Indexed keywords

ALCOHOLS; AMINO ACIDS; BACTERIA; CATALYST ACTIVITY; ENZYMES; PROTEINS;

EID: 0037415359     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00290-9     Document Type: Article
Times cited : (131)

References (29)
  • 1
    • 0348056371 scopus 로고
    • Applications of cofactor dependent enzymes in organic synthesis
    • Carrea G., Riva S. Applications of cofactor dependent enzymes in organic synthesis. Chimica. Oggi. 3:1986;17-21.
    • (1986) Chimica. Oggi. , vol.3 , pp. 17-21
    • Carrea, G.1    Riva, S.2
  • 2
    • 0000697019 scopus 로고
    • Enzyme-catalyzed organic synthesis: A comparison of strategies for in situ regeneration of NAD from NADH
    • Lee L.G., Whitesides G.M. Enzyme-catalyzed organic synthesis: a comparison of strategies for in situ regeneration of NAD from NADH. J. Am. Chem. Soc. 107:1985;6999-7008.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6999-7008
    • Lee, L.G.1    Whitesides, G.M.2
  • 3
    • 0345817539 scopus 로고
    • Regeneration of nicotinamide cofactors for use in organic synthesis
    • Chenault H.K., Whitesides G.M. Regeneration of nicotinamide cofactors for use in organic synthesis. Appl. Biochem. Biotechnol. 14:1987;147-197.
    • (1987) Appl. Biochem. Biotechnol. , vol.14 , pp. 147-197
    • Chenault, H.K.1    Whitesides, G.M.2
  • 4
    • 0030447886 scopus 로고    scopus 로고
    • Chiral alcohols by enantioselective enzymatic oxidation
    • Hummel W., Riebel B. Chiral alcohols by enantioselective enzymatic oxidation. N.Y. Acad. Sci. 799:1996;713-716.
    • (1996) N.Y. Acad. Sci. , vol.799 , pp. 713-716
    • Hummel, W.1    Riebel, B.2
  • 5
    • 0037262411 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis
    • Hummel W, Riebel B. Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis. Biotechnol Lett 2003;25.
    • (2003) Biotechnol Lett , vol.25
    • Hummel, W.1    Riebel, B.2
  • 6
    • 0026525312 scopus 로고
    • Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8
    • Park H.J., Reiser C.O.A., Kondruweit S., Erdmann H., Schmid R.D., Sprinzl M. Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8. Eur. J. Biochem. 205:1992;887-893.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 887-893
    • Park, H.J.1    Reiser, C.O.A.2    Kondruweit, S.3    Erdmann, H.4    Schmid, R.D.5    Sprinzl, M.6
  • 7
    • 0027134889 scopus 로고
    • A flavoprotein functional as NADH oxidase from Amphibacillus xylanus Ep01: Purification and characterization of the enzyme and structural analysis of its gene
    • Niimura Y., Ohnishi K., Yarita Y., Hidaka M., Masaki H., Uchimura T.et al. A flavoprotein functional as NADH oxidase from Amphibacillus xylanus Ep01: purification and characterization of the enzyme and structural analysis of its gene. J. Bacteriol. 175:1993;7945-7950.
    • (1993) J. Bacteriol. , vol.175 , pp. 7945-7950
    • Niimura, Y.1    Ohnishi, K.2    Yarita, Y.3    Hidaka, M.4    Masaki, H.5    Uchimura, T.6
  • 8
    • 0028880854 scopus 로고
    • Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein component
    • Niimura Y., Poole L.B., Massey V. Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein component. J. Biol. Chem. 270:1995;25645-25650.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25645-25650
    • Niimura, Y.1    Poole, L.B.2    Massey, V.3
  • 9
    • 0021951979 scopus 로고
    • Purification and characterization of NADH oxidase from a strain of Leuconostoc mesenteroides
    • Koike K., Kobayashi T., Ito S., Saitoh M. Purification and characterization of NADH oxidase from a strain of Leuconostoc mesenteroides. J. Biochem. Tokyo. 97:1985;1279-1288.
    • (1985) J. Biochem. Tokyo , vol.97 , pp. 1279-1288
    • Koike, K.1    Kobayashi, T.2    Ito, S.3    Saitoh, M.4
  • 10
    • 0026795398 scopus 로고
    • Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases
    • Ross R.P., Claiborne A. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases. J. Mol. Biol. 227:1992;658-671.
    • (1992) J. Mol. Biol. , vol.227 , pp. 658-671
    • Ross, R.P.1    Claiborne, A.2
  • 11
    • 0023907346 scopus 로고
    • NADH oxidase from the extreme thermophile Thermus aquaticus YT-1. Purification and characterisation
    • Cocco D., Rinaldi A., Savini I., Cooper J.M., Bannister J.V. NADH oxidase from the extreme thermophile Thermus aquaticus YT-1. Purification and characterisation. Eur. J. Biochem. 174:1988;267-271.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 267-271
    • Cocco, D.1    Rinaldi, A.2    Savini, I.3    Cooper, J.M.4    Bannister, J.V.5
  • 13
    • 0030801322 scopus 로고    scopus 로고
    • Purification and characterization of Sporolactobacillus inulinus NADH oxidase and its physiological role in aerobic metabolism of the bacterium
    • Nishiyama Y., Massey V., Anzai Y., Watanabe T., Miyaji T., Uchimura T.et al. Purification and characterization of Sporolactobacillus inulinus NADH oxidase and its physiological role in aerobic metabolism of the bacterium. J. Ferment. Bioeng. 84:1997;22-27.
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 22-27
    • Nishiyama, Y.1    Massey, V.2    Anzai, Y.3    Watanabe, T.4    Miyaji, T.5    Uchimura, T.6
  • 14
    • 0019641598 scopus 로고
    • Purification and characterization of NADH oxidase from membranes of Acholeplasma laidlawii, a copper-containing iron-sulfur flavoprotein
    • Reinards R., Kubicki J., Ohlenbusch H. Purification and characterization of NADH oxidase from membranes of Acholeplasma laidlawii, a copper-containing iron-sulfur flavoprotein. Eur. J. Biochem. 120:1981;329-337.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 329-337
    • Reinards, R.1    Kubicki, J.2    Ohlenbusch, H.3
  • 15
    • 0022396889 scopus 로고
    • Purification and properties of NADH oxidase from Bacillus megaterium
    • Saeki Y., Nozaki M., Matsumoto K. Purification and properties of NADH oxidase from Bacillus megaterium. J. Biochem. Tokyo. 98:1985;1433-1440.
    • (1985) J. Biochem. Tokyo , vol.98 , pp. 1433-1440
    • Saeki, Y.1    Nozaki, M.2    Matsumoto, K.3
  • 18
    • 0348056366 scopus 로고    scopus 로고
    • Clontech- http://www.clontech.com/techinfo/manuals/PDF/PT3042-1.pdf .
    • Clontech
  • 19
    • 0030632239 scopus 로고    scopus 로고
    • New alcohol dehydrogenases for the synthesis of chiral compounds
    • Hummel W. New alcohol dehydrogenases for the synthesis of chiral compounds. Adv. Biochem. Eng. Biotechnol. 58:1997;145-184.
    • (1997) Adv. Biochem. Eng. Biotechnol. , vol.58 , pp. 145-184
    • Hummel, W.1
  • 20
    • 0033485581 scopus 로고    scopus 로고
    • Large-scale applications of NAD(P)-dependent oxidoreductases: Recent developments
    • Hummel W. Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol. 12:1999;487-492.
    • (1999) Trends Biotechnol. , vol.12 , pp. 487-492
    • Hummel, W.1
  • 21
    • 0001747792 scopus 로고    scopus 로고
    • Highly regio- and enantioselective reduction of 3,5-dioxocarboxylates
    • Wolberg M., Hummel W., Wandrey C., Müller M. Highly regio- and enantioselective reduction of 3,5-dioxocarboxylates. Angew. Chem. 112:2000;4476-4478.
    • (2000) Angew. Chem. , vol.112 , pp. 4476-4478
    • Wolberg, M.1    Hummel, W.2    Wandrey, C.3    Müller, M.4
  • 22
    • 0012289993 scopus 로고    scopus 로고
    • Biocatalytic reduction of beta delta-diketo esters: A highly stereoselective aproach to all four stereoisomers of a chlorinated beta, delta-dihydroxy hexanoate
    • Wolberg M., Hummel W., Müller M. Biocatalytic reduction of beta delta-diketo esters: a highly stereoselective aproach to all four stereoisomers of a chlorinated beta, delta-dihydroxy hexanoate. Chem. Eur. J. 7:2001;4652-4671.
    • (2001) Chem. Eur. J. , vol.7 , pp. 4652-4671
    • Wolberg, M.1    Hummel, W.2    Müller, M.3
  • 24
    • 0012355073 scopus 로고    scopus 로고
    • Highly enantioselective preparation of multifunctionalized propargylic building blocks
    • Schubert T., Hummel W., Müller M. Highly enantioselective preparation of multifunctionalized propargylic building blocks. Angew. Chem. 114:2002;656-659.
    • (2002) Angew. Chem. , vol.114 , pp. 656-659
    • Schubert, T.1    Hummel, W.2    Müller, M.3
  • 25
    • 0029859396 scopus 로고    scopus 로고
    • Aerobic growth of and activities of NADH oxidase and NADH peroxidase in lactic acid bacteria
    • Sakamoto M., Komagata K. Aerobic growth of and activities of NADH oxidase and NADH peroxidase in lactic acid bacteria. J. Ferment. Bioeng. 82:1996;210-216.
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 210-216
    • Sakamoto, M.1    Komagata, K.2
  • 26
    • 0021260276 scopus 로고
    • Comparison of aerobic and anaerobic growth of Lactobacillus plantarum in a glucose medium
    • Murphy M.G., Condon S. Comparison of aerobic and anaerobic growth of Lactobacillus plantarum in a glucose medium. Arch. Microbiol. 138:1984;49-53.
    • (1984) Arch. Microbiol. , vol.138 , pp. 49-53
    • Murphy, M.G.1    Condon, S.2
  • 27
    • 0021983734 scopus 로고
    • Oxygen dependent lactate utilization by Lactobacillus plantarum
    • Murphy M.G., O'Connor L., Walsh D., Condon S. Oxygen dependent lactate utilization by Lactobacillus plantarum. Arch. Microbiol. 141:1985;75-79.
    • (1985) Arch. Microbiol. , vol.141 , pp. 75-79
    • Murphy, M.G.1    O'Connor, L.2    Walsh, D.3    Condon, S.4
  • 28
    • 0032980780 scopus 로고    scopus 로고
    • Differentiation of Serpulina species by NADH oxidase gene (nox) sequence comparisons and nox-based polymerase chain reaction tests
    • Atyeo R.F., Stanton T.B., Jensen N.S., Suriyaarachichi D.S., Hampson D.J. Differentiation of Serpulina species by NADH oxidase gene (nox) sequence comparisons and nox-based polymerase chain reaction tests. Vet. Microbiol. 67:1999;46-69.
    • (1999) Vet. Microbiol. , vol.67 , pp. 46-69
    • Atyeo, R.F.1    Stanton, T.B.2    Jensen, N.S.3    Suriyaarachichi, D.S.4    Hampson, D.J.5
  • 29
    • 0032748327 scopus 로고    scopus 로고
    • Isolation oxygen sensitivity, and virulence of NADH oxidase mutants of the anaerobic spirochete Brachyspira (Serpulina) hyodysenteriae, etiologic agent of swine dysentery
    • Stanton T.B., Rosey E.L., Kennedy M.J., Jensen N.S., Bosworth B.T. Isolation oxygen sensitivity, and virulence of NADH oxidase mutants of the anaerobic spirochete Brachyspira (Serpulina) hyodysenteriae, etiologic agent of swine dysentery. Appl. Environ. Microbiol. 65:1999;5028-5034.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5028-5034
    • Stanton, T.B.1    Rosey, E.L.2    Kennedy, M.J.3    Jensen, N.S.4    Bosworth, B.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.